eF-site ID 3cy2-AB PDB Code 3cy2 Chain A, B click to enlarge Title Crystal structure of human proto-oncogene serine threonine kinase (PIM1) in complex with a consensus peptide and a beta carboline ligand II Classification TRANSFERASE Compound Proto-oncogene serine/threonine-protein kinase Pim-1, Isoform 2 Source Homo sapiens (Human) (3CY2) Sequence A:  PLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKD RISDWGELPTRVPMEVVLLKKVSSGFSGVIRLLDWFERPD SFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEA VRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLK DTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYD MVCGDIPFEHDEEIIGGQVFFRQRVSSECQHLIRWCLALR PSDRPTFEEIQNHPWMQDVLLPQETAEIHLH B:  RKRRRHPSG Description Functional site 1) chain A residue 67 type sequence K description BINDING SITE FOR RESIDUE CL A 401 source : AC1 2) chain A residue 186 type sequence D description BINDING SITE FOR RESIDUE CL A 401 source : AC1 3) chain A residue 45 type sequence G description BINDING SITE FOR RESIDUE MB9 A 501 source : AC2 4) chain A residue 49 type sequence F description BINDING SITE FOR RESIDUE MB9 A 501 source : AC2 5) chain A residue 67 type sequence K description BINDING SITE FOR RESIDUE MB9 A 501 source : AC2 6) chain A residue 122 type sequence R description BINDING SITE FOR RESIDUE MB9 A 501 source : AC2 7) chain A residue 171 type sequence E description BINDING SITE FOR RESIDUE MB9 A 501 source : AC2 8) chain A residue 172 type sequence N description BINDING SITE FOR RESIDUE MB9 A 501 source : AC2 9) chain A residue 174 type sequence L description BINDING SITE FOR RESIDUE MB9 A 501 source : AC2 10) chain A residue 185 type sequence I description BINDING SITE FOR RESIDUE MB9 A 501 source : AC2 11) chain A residue 186 type sequence D description BINDING SITE FOR RESIDUE MB9 A 501 source : AC2 12) chain A residue 219 type sequence H description BINDING SITE FOR RESIDUE EDO A 551 source : AC3 13) chain A residue 221 type sequence R description BINDING SITE FOR RESIDUE EDO A 551 source : AC3 14) chain A residue 222 type sequence S description BINDING SITE FOR RESIDUE EDO A 551 source : AC3 15) chain A residue 167 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 44 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 44-67 type prosite sequence LGSGGFGSVYSGIRVSDNLPVAIK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGGFGSVYsGirvsdnlp..........VAIK source prosite : PS00107 18) chain A residue 163-175 type prosite sequence VLHRDIKDENILI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDIKdeNILI source prosite : PS00108 19) chain A residue 98 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:15657054 source Swiss-Prot : SWS_FT_FI6 20) chain A residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:15657054 source Swiss-Prot : SWS_FT_FI6 21) chain A residue 67 type BINDING sequence K description BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 121 type BINDING sequence E description BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 128 type BINDING sequence D description BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 source Swiss-Prot : SWS_FT_FI3

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